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Protein

Integrin beta-3

Gene

Itgb3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Integrin alpha-V/beta-3 (ITGAV:ITGB3) is a receptor for cytotactin, fibronectin, laminin, matrix metalloproteinase-2, osteopontin, osteomodulin, prothrombin, thrombospondin, vitronectin and von Willebrand factor. Integrin alpha-IIB/beta-3 (ITGA2B:ITGB3) is a receptor for fibronectin, fibrinogen, plasminogen, prothrombin, thrombospondin and vitronectin. Integrins alpha-IIB/beta-3 and alpha-V/beta-3 recognize the sequence R-G-D in a wide array of ligands. Integrin alpha-IIB/beta-3 recognizes the sequence H-H-L-G-G-G-A-K-Q-A-G-D-V in fibrinogen gamma chain. Following activation integrin alpha-IIB/beta-3 brings about platelet/platelet interaction through binding of soluble fibrinogen. This step leads to rapid platelet aggregation which physically plugs ruptured endothelial surfaces. Fibrinogen binding enhances SELP expression in activated platelets (PubMed:19332769). ITGAV:ITGB3 binds to fractalkine (CX3CL1) and acts as its coreceptor in CX3CR1-dependent fractalkine signaling. ITGAV:ITGB3 binds to NRG1 (via EGF domain) and this binding is essential for NRG1-ERBB signaling. ITGAV:ITGB3 binds to FGF1 and this binding is essential for FGF1 signaling. ITGAV:ITGB3 binds to IGF1 and this binding is essential for IGF1 signaling (By similarity).By similarity1 Publication

GO - Molecular functioni

GO - Biological processi

  • activation of protein kinase activity Source: MGI
  • angiogenesis involved in wound healing Source: InterPro
  • apolipoprotein A-I-mediated signaling pathway Source: MGI
  • cell growth Source: MGI
  • cell-matrix adhesion Source: MGI
  • cell migration Source: MGI
  • cell projection morphogenesis Source: BHF-UCL
  • cell-substrate adhesion Source: MGI
  • cell-substrate junction assembly Source: MGI
  • cellular response to platelet-derived growth factor stimulus Source: MGI
  • heterotypic cell-cell adhesion Source: MGI
  • integrin-mediated signaling pathway Source: MGI
  • negative chemotaxis Source: MGI
  • negative regulation of lipid storage Source: MGI
  • negative regulation of lipid transport Source: MGI
  • negative regulation of lipoprotein metabolic process Source: MGI
  • negative regulation of low-density lipoprotein particle receptor biosynthetic process Source: MGI
  • negative regulation of macrophage derived foam cell differentiation Source: MGI
  • platelet activation Source: MGI
  • platelet aggregation Source: MGI
  • platelet-derived growth factor receptor signaling pathway Source: MGI
  • positive regulation of bone resorption Source: BHF-UCL
  • positive regulation of cell-matrix adhesion Source: MGI
  • positive regulation of cell migration Source: BHF-UCL
  • positive regulation of endothelial cell migration Source: MGI
  • positive regulation of endothelial cell proliferation Source: MGI
  • positive regulation of fibroblast migration Source: MGI
  • positive regulation of fibroblast proliferation Source: MGI
  • positive regulation of gene expression Source: UniProtKB
  • positive regulation of osteoblast proliferation Source: BHF-UCL
  • positive regulation of osteoclast differentiation Source: BHF-UCL
  • positive regulation of peptidyl-tyrosine phosphorylation Source: MGI
  • positive regulation of substrate adhesion-dependent cell spreading Source: MGI
  • positive regulation of T cell migration Source: UniProtKB
  • protein folding Source: MGI
  • regulation of actin cytoskeleton organization Source: UniProtKB
  • regulation of cell migration Source: MGI
  • regulation of extracellular matrix organization Source: MGI
  • regulation of protein tyrosine kinase activity Source: MGI
  • smooth muscle cell migration Source: MGI
  • substrate adhesion-dependent cell spreading Source: MGI
  • viral entry into host cell Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Integrin, Receptor

Keywords - Biological processi

Cell adhesion

Enzyme and pathway databases

ReactomeiR-MMU-114608. Platelet degranulation.
R-MMU-1566948. Elastic fibre formation.
R-MMU-2129379. Molecules associated with elastic fibres.
R-MMU-216083. Integrin cell surface interactions.
R-MMU-3000170. Syndecan interactions.
R-MMU-3000178. ECM proteoglycans.
R-MMU-354192. Integrin alphaIIb beta3 signaling.
R-MMU-354194. GRB2:SOS provides linkage to MAPK signaling for Integrins.
R-MMU-372708. p130Cas linkage to MAPK signaling for integrins.
R-MMU-4420097. VEGFA-VEGFR2 Pathway.
R-MMU-445144. Signal transduction by L1.

Names & Taxonomyi

Protein namesi
Recommended name:
Integrin beta-3
Alternative name(s):
Platelet membrane glycoprotein IIIa
Short name:
GPIIIa
CD_antigen: CD61
Gene namesi
Name:Itgb3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:96612. Itgb3.

Subcellular locationi

  • Cell membrane By similarity; Single-pass type I membrane protein By similarity
  • Cell projectionlamellipodium membrane By similarity
  • Cell junctionfocal adhesion By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini26 – 717692ExtracellularSequence analysisAdd
BLAST
Transmembranei718 – 74023HelicalSequence analysisAdd
BLAST
Topological domaini741 – 78747CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • alpha9-beta1 integrin-ADAM8 complex Source: BHF-UCL
  • apical plasma membrane Source: MGI
  • cell surface Source: UniProtKB
  • external side of plasma membrane Source: MGI
  • extracellular exosome Source: MGI
  • filopodium membrane Source: MGI
  • focal adhesion Source: MGI
  • integrin alpha9-beta1 complex Source: BHF-UCL
  • integrin alphav-beta3 complex Source: MGI
  • integrin complex Source: MGI
  • lamellipodium membrane Source: MGI
  • melanosome Source: MGI
  • microvillus membrane Source: MGI
  • nucleus Source: MGI
  • plasma membrane Source: MGI
  • receptor complex Source: MGI
  • ruffle membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2525Sequence analysisAdd
BLAST
Chaini26 – 787762Integrin beta-3PRO_0000016345Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi30 ↔ 460By similarity
Disulfide bondi38 ↔ 48By similarity
Disulfide bondi41 ↔ 74By similarity
Disulfide bondi51 ↔ 63By similarity
Disulfide bondi202 ↔ 209By similarity
Disulfide bondi257 ↔ 298By similarity
Glycosylationi345 – 3451N-linked (GlcNAc...)Sequence analysis
Glycosylationi396 – 3961N-linked (GlcNAc...)Sequence analysis
Disulfide bondi399 ↔ 411By similarity
Disulfide bondi431 ↔ 680By similarity
Disulfide bondi458 ↔ 462By similarity
Disulfide bondi473 ↔ 485By similarity
Glycosylationi477 – 4771N-linked (GlcNAc...)Sequence analysis
Disulfide bondi482 ↔ 520By similarity
Disulfide bondi487 ↔ 496By similarity
Disulfide bondi498 ↔ 511By similarity
Disulfide bondi526 ↔ 531By similarity
Disulfide bondi528 ↔ 561By similarity
Disulfide bondi533 ↔ 546By similarity
Disulfide bondi548 ↔ 553By similarity
Disulfide bondi567 ↔ 572By similarity
Disulfide bondi569 ↔ 600By similarity
Disulfide bondi574 ↔ 583By similarity
Glycosylationi584 – 5841N-linked (GlcNAc...)Sequence analysis
Disulfide bondi585 ↔ 592By similarity
Disulfide bondi606 ↔ 611By similarity
Disulfide bondi608 ↔ 656By similarity
Disulfide bondi613 ↔ 623By similarity
Disulfide bondi626 ↔ 629By similarity
Disulfide bondi633 ↔ 642By similarity
Disulfide bondi639 ↔ 712By similarity
Disulfide bondi660 ↔ 688By similarity
Glycosylationi679 – 6791N-linked (GlcNAc...)Sequence analysis
Modified residuei766 – 7661PhosphothreonineCombined sources
Modified residuei772 – 7721PhosphotyrosineBy similarity
Modified residuei778 – 7781PhosphothreonineBy similarity
Modified residuei784 – 7841PhosphotyrosineBy similarity

Post-translational modificationi

Phosphorylated on tyrosine residues in response to thrombin-induced platelet aggregation. Probably involved in outside-in signaling.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

EPDiO54890.
MaxQBiO54890.
PaxDbiO54890.
PRIDEiO54890.

PTM databases

iPTMnetiO54890.
PhosphoSiteiO54890.

Expressioni

Gene expression databases

BgeeiO54890.
CleanExiMM_ITGB3.
GenevisibleiO54890. MM.

Interactioni

Subunit structurei

Heterodimer of an alpha and a beta subunit (By similarity). Beta-3 (ITGB3) associates with either alpha-IIB (ITGA2B) or alpha-V (ITGAV). Interacts with FLNB and COMP (By similarity). Interacts with PDIA6 following platelet stimulation (By similarity). Interacts with SYK; upon activation by ITGB3 promotes platelet adhesion (By similarity). Interacts with MYO10 (By similarity). Interacts with DAB2 (PubMed:12606711). Interacts with FERMT2 (PubMed:18483218). Integrin ITGAV:ITGB3 interacts with FBLN5 (via N-terminus) (PubMed:11805835). Interacts with EMP2; regulates the levels of the heterodimer ITGA5:ITGB3 integrin expression on the plasma membrane (By similarity). ITGAV:ITGB3 interacts with NOV (By similarity). ITGAV:ITGB3 interacts with AGRA2 (By similarity). ITGAV:ITGB3 is found in a ternary complex with CX3CR1 and CX3CL1. ITGAV:ITGB3 is found in a ternary complex with NRG1 and ERBB3. ITGAV:ITGB3 is found in a ternary complex with FGF1 and FGFR1. ITGAV:ITGB3 is found in a ternary complex with IGF1 and IGF1R (By similarity).By similarity3 Publications

GO - Molecular functioni

Protein-protein interaction databases

BioGridi200830. 3 interactions.
DIPiDIP-46416N.
IntActiO54890. 4 interactions.
MINTiMINT-4099028.
STRINGi10090.ENSMUSP00000021028.

Structurei

3D structure databases

ProteinModelPortaliO54890.
SMRiO54890. Positions 28-787.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini134 – 376243VWFAAdd
BLAST
Repeati462 – 51049IAdd
BLAST
Repeati511 – 55242IIAdd
BLAST
Repeati553 – 59139IIIAdd
BLAST
Repeati592 – 62837IVAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni202 – 2098CX3CL1-bindingBy similarity
Regioni202 – 2098Involved in CX3CL1-, NRG1-, FGF1- and IGF1-bindingBy similarity
Regioni292 – 31221CX3CL1-bindingBy similarityAdd
BLAST
Regioni462 – 628167Cysteine-rich tandem repeatsAdd
BLAST

Sequence similaritiesi

Belongs to the integrin beta chain family.Curated
Contains 1 VWFA domain.Curated

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1226. Eukaryota.
ENOG410XP60. LUCA.
GeneTreeiENSGT00760000119064.
HOGENOMiHOG000252936.
HOVERGENiHBG006190.
InParanoidiO54890.
KOiK06493.
OMAiGHGQCSC.
OrthoDBiEOG7T7GSB.
TreeFamiTF105392.

Family and domain databases

Gene3Di1.20.5.630. 1 hit.
3.40.50.410. 1 hit.
InterProiIPR013111. EGF_extracell.
IPR027068. Integrin_beta-3.
IPR015812. Integrin_bsu.
IPR014836. Integrin_bsu_cyt_dom.
IPR002369. Integrin_bsu_N.
IPR012896. Integrin_bsu_tail.
IPR032695. Integrin_dom.
IPR016201. Plexin-like_fold.
IPR002035. VWF_A.
[Graphical view]
PANTHERiPTHR10082. PTHR10082. 1 hit.
PTHR10082:SF25. PTHR10082:SF25. 1 hit.
PfamiPF07974. EGF_2. 2 hits.
PF08725. Integrin_b_cyt. 1 hit.
PF07965. Integrin_B_tail. 1 hit.
PF00362. Integrin_beta. 1 hit.
[Graphical view]
PIRSFiPIRSF002512. Integrin_B. 1 hit.
PRINTSiPR01186. INTEGRINB.
SMARTiSM00187. INB. 1 hit.
SM01241. Integrin_b_cyt. 1 hit.
SM01242. Integrin_B_tail. 1 hit.
SM00423. PSI. 1 hit.
[Graphical view]
SUPFAMiSSF103575. SSF103575. 1 hit.
SSF53300. SSF53300. 1 hit.
SSF69179. SSF69179. 1 hit.
SSF69687. SSF69687. 1 hit.
PROSITEiPS00022. EGF_1. 2 hits.
PS01186. EGF_2. 1 hit.
PS00243. INTEGRIN_BETA. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O54890-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRAQWPGQLW AALLALGALA GVVVGESNIC TTRGVNSCQQ CLAVSPVCAW
60 70 80 90 100
CSDETLSQGS PRCNLKENLL KDNCAPESIE FPVSEAQILE ARPLSSKGSG
110 120 130 140 150
SSAQITQVSP QRIALRLRPD DSKIFSLQVR QVEDYPVDIY YLMDLSFSMK
160 170 180 190 200
DDLSSIQTLG TKLASQMRKL TSNLRIGFGA FVDKPVSPYM YISPPQAIKN
210 220 230 240 250
PCYNMKNACL PMFGYKHVLT LTDQVSRFNE EVKKQSVSRN RDAPEGGFDA
260 270 280 290 300
IMQATVCDEK IGWRNDASHL LVFTTDAKTH IALDGRLAGI VLPNDGHCHI
310 320 330 340 350
GTDNHYSAST TMDYPSLGLM TEKLSQKNIN LIFAVTENVV SLYQNYSELI
360 370 380 390 400
PGTTVGVLSD DSSNVLQLIV DAYGKIRSKV ELEVRDLPEE LSLSFNATCL
410 420 430 440 450
NNEVIPGLKS CVGLKIGDTV SFSIEAKVRG CPQEKEQSFT IKPVGFKDSL
460 470 480 490 500
TVQVTFDCDC ACQAFAQPSS PRCNNGNGTF ECGVCRCDQG WLGSMCECSE
510 520 530 540 550
EDYRPSQQEE CSPKEGQPIC SQRGECLCGQ CVCHSSDFGK ITGKYCECDD
560 570 580 590 600
FSCVRYKGEM CSGHGQCNCG DCVCDSDWTG YYCNCTTRTD TCMSTNGLLC
610 620 630 640 650
SGRGNCECGS CVCVQPGSYG DTCEKCPTCP DACSFKKECV ECKKFNRGTL
660 670 680 690 700
HEENTCSRYC RDDIEQVKEL TDTGKNAVNC TYKNEDDCVV RFQYYEDTSG
710 720 730 740 750
RAVLYVVEEP ECPKGPDILV VLLSVMGAIL LIGLATLLIW KLLITIHDRK
760 770 780
EFAKFEEERA RAKWDTANNP LYKEATSTFT NITYRGT
Length:787
Mass (Da):86,738
Last modified:July 27, 2011 - v2
Checksum:i4F2E606969788794
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti114 – 1141A → V in AAB94086 (Ref. 1) Curated
Sequence conflicti389 – 3891E → G in AAB94086 (Ref. 1) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF026509 mRNA. Translation: AAB94086.1.
AK157958 mRNA. Translation: BAE34283.1.
AL603709, BX000996 Genomic DNA. Translation: CAM22629.1.
BX000996, AL603709 Genomic DNA. Translation: CAM27926.1.
CH466558 Genomic DNA. Translation: EDL34227.1.
BC125518 mRNA. Translation: AAI25519.1.
BC125520 mRNA. Translation: AAI25521.1.
CCDSiCCDS25536.1.
PIRiPN0510.
RefSeqiNP_058060.2. NM_016780.2.
UniGeneiMm.87150.

Genome annotation databases

EnsembliENSMUST00000021028; ENSMUSP00000021028; ENSMUSG00000020689.
GeneIDi16416.
KEGGimmu:16416.
UCSCiuc007lwx.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF026509 mRNA. Translation: AAB94086.1.
AK157958 mRNA. Translation: BAE34283.1.
AL603709, BX000996 Genomic DNA. Translation: CAM22629.1.
BX000996, AL603709 Genomic DNA. Translation: CAM27926.1.
CH466558 Genomic DNA. Translation: EDL34227.1.
BC125518 mRNA. Translation: AAI25519.1.
BC125520 mRNA. Translation: AAI25521.1.
CCDSiCCDS25536.1.
PIRiPN0510.
RefSeqiNP_058060.2. NM_016780.2.
UniGeneiMm.87150.

3D structure databases

ProteinModelPortaliO54890.
SMRiO54890. Positions 28-787.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi200830. 3 interactions.
DIPiDIP-46416N.
IntActiO54890. 4 interactions.
MINTiMINT-4099028.
STRINGi10090.ENSMUSP00000021028.

PTM databases

iPTMnetiO54890.
PhosphoSiteiO54890.

Proteomic databases

EPDiO54890.
MaxQBiO54890.
PaxDbiO54890.
PRIDEiO54890.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000021028; ENSMUSP00000021028; ENSMUSG00000020689.
GeneIDi16416.
KEGGimmu:16416.
UCSCiuc007lwx.2. mouse.

Organism-specific databases

CTDi3690.
MGIiMGI:96612. Itgb3.

Phylogenomic databases

eggNOGiKOG1226. Eukaryota.
ENOG410XP60. LUCA.
GeneTreeiENSGT00760000119064.
HOGENOMiHOG000252936.
HOVERGENiHBG006190.
InParanoidiO54890.
KOiK06493.
OMAiGHGQCSC.
OrthoDBiEOG7T7GSB.
TreeFamiTF105392.

Enzyme and pathway databases

ReactomeiR-MMU-114608. Platelet degranulation.
R-MMU-1566948. Elastic fibre formation.
R-MMU-2129379. Molecules associated with elastic fibres.
R-MMU-216083. Integrin cell surface interactions.
R-MMU-3000170. Syndecan interactions.
R-MMU-3000178. ECM proteoglycans.
R-MMU-354192. Integrin alphaIIb beta3 signaling.
R-MMU-354194. GRB2:SOS provides linkage to MAPK signaling for Integrins.
R-MMU-372708. p130Cas linkage to MAPK signaling for integrins.
R-MMU-4420097. VEGFA-VEGFR2 Pathway.
R-MMU-445144. Signal transduction by L1.

Miscellaneous databases

ChiTaRSiItgb3. mouse.
PROiO54890.
SOURCEiSearch...

Gene expression databases

BgeeiO54890.
CleanExiMM_ITGB3.
GenevisibleiO54890. MM.

Family and domain databases

Gene3Di1.20.5.630. 1 hit.
3.40.50.410. 1 hit.
InterProiIPR013111. EGF_extracell.
IPR027068. Integrin_beta-3.
IPR015812. Integrin_bsu.
IPR014836. Integrin_bsu_cyt_dom.
IPR002369. Integrin_bsu_N.
IPR012896. Integrin_bsu_tail.
IPR032695. Integrin_dom.
IPR016201. Plexin-like_fold.
IPR002035. VWF_A.
[Graphical view]
PANTHERiPTHR10082. PTHR10082. 1 hit.
PTHR10082:SF25. PTHR10082:SF25. 1 hit.
PfamiPF07974. EGF_2. 2 hits.
PF08725. Integrin_b_cyt. 1 hit.
PF07965. Integrin_B_tail. 1 hit.
PF00362. Integrin_beta. 1 hit.
[Graphical view]
PIRSFiPIRSF002512. Integrin_B. 1 hit.
PRINTSiPR01186. INTEGRINB.
SMARTiSM00187. INB. 1 hit.
SM01241. Integrin_b_cyt. 1 hit.
SM01242. Integrin_B_tail. 1 hit.
SM00423. PSI. 1 hit.
[Graphical view]
SUPFAMiSSF103575. SSF103575. 1 hit.
SSF53300. SSF53300. 1 hit.
SSF69179. SSF69179. 1 hit.
SSF69687. SSF69687. 1 hit.
PROSITEiPS00022. EGF_1. 2 hits.
PS01186. EGF_2. 1 hit.
PS00243. INTEGRIN_BETA. 3 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. McHugh K.P., Teitelbaum S.L., Kitazawa S., Ross F.P.
    Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C3H/HeN.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Inner ear.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  6. Cited for: INTERACTION WITH FBLN5.
  7. "Integrin beta cytoplasmic domain interactions with phosphotyrosine-binding domains: a structural prototype for diversity in integrin signaling."
    Calderwood D.A., Fujioka Y., de Pereda J.M., Garcia-Alvarez B., Nakamoto T., Margolis B., McGlade C.J., Liddington R.C., Ginsberg M.H.
    Proc. Natl. Acad. Sci. U.S.A. 100:2272-2277(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DAB2.
  8. "Kindlin-2 controls bidirectional signaling of integrins."
    Montanez E., Ussar S., Schifferer M., Bosl M., Zent R., Moser M., Fassler R.
    Genes Dev. 22:1325-1330(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FERMT2.
  9. "Fibrinogen is required for maintenance of platelet intracellular and cell-surface P-selectin expression."
    Yang H., Lang S., Zhai Z., Li L., Kahr W.H., Chen P., Brkic J., Spring C.M., Flick M.J., Degen J.L., Freedman J., Ni H.
    Blood 114:425-436(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-766, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brown adipose tissue, Kidney, Liver, Lung and Spleen.

Entry informationi

Entry nameiITB3_MOUSE
AccessioniPrimary (citable) accession number: O54890
Secondary accession number(s): Q3TZC6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: July 27, 2011
Last modified: June 8, 2016
This is version 146 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.